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IUBMB Comments The enzyme, characterized from the bacterium Escherichia coli , catalyses three hydroxylation reactions in the oxygen-independent pathway for ubiquinone (UQ) biosynthesis. The reaction involves an electron acceptor whose identity remains unknown as of 2024. The Escherichia coli enzyme is a heterodimer, with both subunits containing a [4Fe-4S]
Reaction Schemes
a 2-(all-trans-polyprenyl)phenol
+
+
=
a 3-(all-trans-polyprenyl)benzene-1,2-diol
+
+
+
a 2-methoxy-6-(all-trans-polyprenyl)phenol
+
+
=
a 2-methoxy-6-(all-trans-polyprenyl)benzene-1,4-diol
+
+
+
a 5-methoxy-2-methyl-3-(all-trans-polyprenyl)benzene-1,4-diol
+
+
=
a 3-demethylubiquinol
+
+
+
Synonyms
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ubiquinone hydroxylase UbiUV
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a 2-(all-trans-polyprenyl)phenol + prephenate + acceptor = a 3-(all-trans-polyprenyl)benzene-1,2-diol + 3-phenyl-2-oxopropanoate + CO2 + reduced acceptor
(1)
-
-
-
a 2-methoxy-6-(all-trans-polyprenyl)phenol + prephenate + acceptor = a 2-methoxy-6-(all-trans-polyprenyl)benzene-1,4-diol + 3-phenyl-2-oxopropanoate + CO2 + reduced acceptor
(2)
-
-
-
a 5-methoxy-2-methyl-3-(all-trans-polyprenyl)benzene-1,4-diol + prephenate + acceptor = a 3-demethylubiquinol + 3-phenyl-2-oxopropanoate + CO2 + reduced acceptor
(3)
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-
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prephenate,acceptor:2-(all-trans-polyprenyl)phenol oxidoreductase (6-hydroxylating)
The enzyme, characterized from the bacterium Escherichia coli, catalyses three hydroxylation reactions in the oxygen-independent pathway for ubiquinone (UQ) biosynthesis. The reaction involves an electron acceptor whose identity remains unknown as of 2024. The Escherichia coli enzyme is a heterodimer, with both subunits containing a [4Fe-4S] cluster that is essential for activity and may serve as part of an electron transfer chain from the substrate to the unidentified electron acceptor.
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a 2-(all-trans-polyprenyl)phenol + prephenate + acceptor
a 3-(all-trans-polyprenyl)benzene-1,2-diol + 3-phenyl-2-oxopropanoate + CO2 + reduced acceptor
P45527; P45475
Substrates: -
?
a 2-methoxy-6-(all-trans-polyprenyl)phenol + prephenate + acceptor
a 2-methoxy-6-(all-trans-polyprenyl)benzene-1,4-diol + 3-phenyl-2-oxopropanoate + CO2 + reduced acceptor
P45527; P45475
Substrates: -
?
a 5-methoxy-2-methyl-3-(all-trans-polyprenyl)benzene-1,4-diol + prephenate + acceptor
a 3-demethylubiquinol + 3-phenyl-2-oxopropanoate + CO2 + reduced acceptor
P45527; P45475
Substrates: -
?
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a 2-(all-trans-polyprenyl)phenol + prephenate + acceptor
a 3-(all-trans-polyprenyl)benzene-1,2-diol + 3-phenyl-2-oxopropanoate + CO2 + reduced acceptor
P45527; P45475
Substrates: -
?
a 2-methoxy-6-(all-trans-polyprenyl)phenol + prephenate + acceptor
a 2-methoxy-6-(all-trans-polyprenyl)benzene-1,4-diol + 3-phenyl-2-oxopropanoate + CO2 + reduced acceptor
P45527; P45475
Substrates: -
?
a 5-methoxy-2-methyl-3-(all-trans-polyprenyl)benzene-1,4-diol + prephenate + acceptor
a 3-demethylubiquinol + 3-phenyl-2-oxopropanoate + CO2 + reduced acceptor
P45527; P45475
Substrates: -
?
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4Fe-4S-center
P45527; P45475
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4Fe-4S-center
P45527; P45475
UbiU and UbiV each contain an iron-sulfur ([4Fe-4S]) cluster coordinated by four conserved cysteine residues embedded in the so-called protease U32 domain
4Fe-4S-center
P45527; P45475
UbiU-UbiV form a heterodimer, wherein each protein binds a 4Fe-4S cluster via conserved cysteines that are essential for activity
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P45527: ubiquinone biosynthesis protein UbiU, P45475: ubiquinone biosynthesis protein UbiV
P45527; P45475
SwissProt
brenda
P45527: ubiquinone biosynthesis protein UbiU, P45475: ubiquinone biosynthesis protein UbiV; substrain MG1655
P45527; P45475
SwissProt
brenda
Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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metabolism
P45527; P45475
the enzyme catalyses three hydroxylation reactions in the oxygen-independent pathway for ubiquinone biosynthesis
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heterodimer
P45527; P45475
UbiU-UbiV form a heterodimer
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expression in Escherichia coli BL21(DE3)
P45527; P45475
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Fnr activates ubiUV transcription under anaerobiosis
P45527; P45475
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Pelosi, L.; Vo, C.; Abby, S.; Loiseau, L.; Rascalou, B.; Chehade, M.; Faivre, B.; Gousse, M.; Chenal, C.; Touati, N.; Binet, L.; Cornu, D.; Fyfe, C.; Fontecave, M.; Barras, F.; Lombard, M.; Pierrel, F.
Ubiquinone biosynthesis over the entire O2 range Characterization of a conserved O2-independent pathway
mBio
10
e01319-19
2019
Escherichia coli (P45527 AND P45475)
brenda
Arias-Cartin, R.; Kazemzadeh Ferizhendi, K.; Sechet, E.; Pelosi, L.; Loeuillet, C.; Pierrel, F.; Barras, F.; Bouveret, E.
Role of the Escherichia coli ubiquinone-synthesizing UbiUVT pathway in adaptation to changing respiratory conditions
mBio
14
e0329822
2023
Escherichia coli (P45527 AND P45475)
brenda
Ferizhendi, K.; Simon, P.; Pelosi, L.; Sechet, E.; Arulanandam, R.; Chehade, M.; Rey, M.; Onal, D.; Flandrin, L.; Chreim, R.; Faivre, B.; Chau-Duy-Tam Vo, S.; Arias-Cartin, R.; Barras, F.; Fontecave, M.; Bouveret, E.; Lombard, M.; Pierrel, F.
An organic O donor for biological hydroxylation reactions
Proc. Natl. Acad. Sci. USA
121
e2321242121
2024
Escherichia coli (P45527 AND P45475)
brenda
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